SASDQD8 – Rap guanine nucleotide exchange factor Epac1 with cAMP and CE3F4 inhibitor

Rap guanine nucleotide exchange factor 3 experimental SAS data
Rap guanine nucleotide exchange factor 3 Kratky plot
Sample: Rap guanine nucleotide exchange factor 3 monomer, 82 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 0.5 mM EDTA, pH: 8
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Oct 4
Membranes prime the RapGEF EPAC1 to transduce cAMP signaling Nature Communications 14(1) (2023)
Sartre C, Peurois F, Ley M, Kryszke M, Zhang W, Courilleau D, Fischmeister R, Ambroise Y, Zeghouf M, Cianferani S, Ferrandez Y, Cherfils J
RgGuinier 3.3 nm
Dmax 11.8 nm
VolumePorod 134 nm3

SASDPV7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (no reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 10
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 59 nm3

SASDPW7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (with reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 30 mM DTT, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 7
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 64 nm3

SASDLK7 – Bartonella effector protein (Bep1), 15 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2020 May 29
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 4.1 nm
Dmax 13.4 nm
VolumePorod 83 nm3

SASDLL7 – Bartonella effector protein (Bep1), 20 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 3.8 nm
Dmax 13.4 nm
VolumePorod 87 nm3

SASDLM7 – Bartonella effector protein (Bep1), 35 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 108 nm3

SASDRE6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047)

Ras GTPase-activating protein 1 experimental SAS data
ALPHAFOLD model
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 14.0 nm
VolumePorod 172 nm3

SASDRF6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to doubly phosphorylated EphB4 peptide

Ephrin type-B receptor 4Ras GTPase-activating protein 1 experimental SAS data
Ephrin type-B receptor 4 Ras GTPase-activating protein 1 Kratky plot
Sample: Ephrin type-B receptor 4 monomer, 2 kDa Homo sapiens protein
Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 3.9 nm
Dmax 13.7 nm
VolumePorod 176 nm3

SASDRG6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to doubly phosphorylated p190RhoGAP peptide

Rho GTPase-activating protein 35Ras GTPase-activating protein 1 experimental SAS data
Rho GTPase-activating protein 35 Ras GTPase-activating protein 1 Kratky plot
Sample: Rho GTPase-activating protein 35 monomer, 3 kDa Homo sapiens protein
Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 15.1 nm
VolumePorod 194 nm3

SASDRH6 – Ras GTPase-activating protein 1 (p120RasGAP, amino acids 174–1047) bound to a doubly phosphorylated Dok1 peptide

Ras GTPase-activating protein 1Docking protein 1 experimental SAS data
Ras GTPase-activating protein 1 Docking protein 1 Kratky plot
Sample: Ras GTPase-activating protein 1 monomer, 101 kDa Homo sapiens protein
Docking protein 1 monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2021 Nov 4
Diverse p120RasGAP interactions with doubly phosphorylated partners EphB4, p190RhoGAP and Dok1 Journal of Biological Chemistry :105098 (2023)
Vish K, Stiegler A, Boggon T
RgGuinier 4.0 nm
Dmax 14.6 nm
VolumePorod 196 nm3

4692 hits found.